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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
1994-8-31
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pubmed:abstractText |
Studies were undertaken to compare the signal-induced redistribution of conventional protein kinase C (cPKC) to nonclassical protein kinase C (nPKC) family members in response to phorbol 12-myristate 13-acetate (PMA) or nerve growth factor (NGF) treatment of PC12 cells. cPKC-alpha and -beta and nPKC-delta and -epsilon were predominantly cytoplasmic, whereas PKC-zeta displayed approximately equal distribution between the cytoplasm and membrane fraction. Treatment of PC12 cells with PMA induced rapid translocation of both c- and nPKC isoforms to the membrane fraction, although the kinetics varied between isoforms with epsilon being most sensitive, followed by delta > zeta > alpha. Both PKC-epsilon and delta translocated in the presence of minute concentrations of PMA, whereas cPKC was less sensitive, and PKC-zeta was least sensitive. NGF treatment, on the other hand, induced translocation of cPKCs and delta and epsilon nPKC, albeit with differential magnitude, whereas PKC-zeta was found predominantly in the cytoplasm. Chronic treatment of PC12 cells with PMA (1 microM) caused a rapid disappearance of alpha, beta, delta, and epsilon PKC isoforms, whereas the expression of PKC-zeta was unaltered over 4 days. NGF induced an increase in cytoplasmic PKC-zeta in control, or PMA down-regulated PC12 cells. Moreover, the increase in cytoplasmic PKC-zeta was blocked by pretreatment with sphingosine (2.5 microM). Furthermore, PKC-zeta was activated by NGF in PMA down-regulated PC12 cells, as determined by the extent of epsilon-peptide phosphorylation using a permeabilized cell assay. In addition, the zeta-pseudosubstrate peptide inhibited NGF-induced activation of PKC-zeta.(ABSTRACT TRUNCATED AT 250 WORDS)
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Growth Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Tetradecanoylphorbol Acetate,
http://linkedlifedata.com/resource/pubmed/chemical/protein kinase C zeta
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1044-9523
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
395-403
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pubmed:dateRevised |
2009-4-7
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pubmed:meshHeading |
pubmed-meshheading:8043513-Animals,
pubmed-meshheading:8043513-Cell Differentiation,
pubmed-meshheading:8043513-Enzyme Activation,
pubmed-meshheading:8043513-Isoenzymes,
pubmed-meshheading:8043513-Nerve Growth Factors,
pubmed-meshheading:8043513-Neurites,
pubmed-meshheading:8043513-PC12 Cells,
pubmed-meshheading:8043513-Protein Kinase C,
pubmed-meshheading:8043513-Rats,
pubmed-meshheading:8043513-Rats, Sprague-Dawley,
pubmed-meshheading:8043513-Signal Transduction,
pubmed-meshheading:8043513-Subcellular Fractions,
pubmed-meshheading:8043513-Tetradecanoylphorbol Acetate
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pubmed:year |
1994
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pubmed:articleTitle |
A role for zeta protein kinase C in nerve growth factor-induced differentiation of PC12 cells.
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pubmed:affiliation |
Department of Zoology, Auburn University, Alabama 36849.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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